ArticleChembiochem : a European journal of chemical biology2021
Discovery of an Allosteric Ligand Binding Site in SMYD3 Lysine Methyltransferase.
Article in Chembiochem : a European journal of chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
10 citing papers in PubMed.
- Breaking the boundaries of affinity selection-mass spectrometry: From ligand screening to target-ligand interaction insights.Journal of pharmaceutical analysis · 2026Review
- Therapeutic Targeting of Protein Lysine and Arginine Methyltransferases: Principles and Strategies for Inhibitor Design.International journal of molecular sciences · 2025Review
- Identification of fragments targeting SMYD3 using highly sensitive kinetic and multiplexed biosensor-based screening.RSC medicinal chemistry · 2024Article
- Promiscuous Enzymes for Residue-Specific Peptide and Protein Late-Stage Functionalization.Chembiochem : a European journal of chemical biology · 2023Review
- Data-driven analysis and druggability assessment methods to accelerate the identification of novel cancer targets.Computational and structural biotechnology journal · 2023Review
- Computational Design of Inhibitors Targeting the Catalytic β Subunit ofAntibiotics (Basel, Switzerland) · 2022Article
- Lysine methyltransferase inhibitors: where we are now.RSC chemical biology · 2022Review
- Exploring the druggability of the binding site of aurovertin, an exogenous allosteric inhibitor of FFrontiers in pharmacology · 2022Article
- Playing on the Dark Side: SMYD3 Acts as a Cancer Genome Keeper in Gastrointestinal Malignancies.Cancers · 2021Review
- Discovery of an Allosteric Ligand Binding Site in SMYD3 Lysine Methyltransferase.Chembiochem : a European journal of chemical biology · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
19 authors.
Funding
Abstract
SMYD3 is a multifunctional epigenetic enzyme with lysine methyltransferase activity and various interaction partners. It is implicated in the pathophysiology of cancers but with an unclear mechanism. To discover tool compounds for clarifying its biochemistry and potential as a therapeutic target, a set of drug-like compounds was screened in a biosensor-based competition assay. Diperodon was identified as an allosteric ligand; its R and S enantiomers were isolated, and their affinities to SMYD3 were determined (K
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.